Cited by 198Cell death mechanisms and regulationInflammasome and immune disordersEnzyme Structure and Function

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Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex

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Fu, Tian-Min, Li, Yang, Lu, Alvin, Li, Zongli, Vajjhala, Parimala R., Cruz, Anthony C., Srivastava, Devendra B., DiMaio, Frank, Penczek, Pawel A., Siegel, Richard M., Stacey, Katryn J., Egelman, Edward H., Wu, Hao·2016·Molecular Cell

DOI 10.1016/j.molcel.2016.09.009PMC PMC5089849

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Abstract

Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC. Caspase-8 assembles with FADD at the DISC and with ASC at the inflammasome through its tandem death effector domain (tDED), which is regulated by the tDED-containing cellular inhibitor cFLIP and the viral inhibitor MC159. Here we present the caspase-8 tDED filament structure determined by cryoelectron microscopy. Extensive assembly interfaces not predicted by the previously proposed linear DED chain model were uncovered, and were further confirmed by structure-based mutagenesis in filament formation in vitro and Fas-induced apoptosis and ASC-mediated caspase-8 recruitment in cells. Structurally, the two DEDs in caspase-8 use quasi-equivalent contacts to enable assembly. Using the tDED filament structure as a template, structural analyses reveal the interaction surfaces between FADD and caspase-8 and the distinct mechanisms of regulation by cFLIP and MC159 through comingling and capping, respectively.

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Biasini, M., Bienert, S., Waterhouse, A. M., Arnold, K., Studer, G., Schmidt, T., Kiefer, F., Cassarino, T. G., Bertoni, M., Bordoli, L., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku340 · Cited by 4,709
The TNF and TNF Receptor Superfamilies
Locksley, R. M., Killeen, N., & Lenardo, M. J. (2001) · Cell · doi:10.1016/s0092-8674(01)00237-9 · Cited by 3,650
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627
Cytotoxicity‐dependent APO‐1 (Fas/CD95)‐associated proteins form a death‐inducing signaling complex (DISC) with the receptor.
Kischkel, F. C., Hellbardt, S., Behrmann, I., Germer, M., Pawlita, M., Krammer, P. H., & Peter, M. E. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00245.x · Cited by 2,181
Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes
Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schröder, G. F., Fitzgerald, K. A., Wu, H., & Egelman, E. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.008 · Cited by 1,353
Self-citation
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Lin, S.-C., Lo, Y.-C., & Wu, H. (2010) · Nature · doi:10.1038/nature09121 · Cited by 1,111
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Boatright, K. M., Renatus, M., Scott, F. L., Sperandio, S., Shin, H., Pedersen, I. M., Ricci, J., Edris, W. A., Sutherlin, D. P., Green, D. R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00051-0 · Cited by 986
The many roles of FAS receptor signaling in the immune system
Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968
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Self-citation
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König, C., & Lavrik, I. N. (2025) · STAR Protocols · doi:10.1016/j.xpro.2025.104131
Apoptosis
Wible, D. J., & Bratton, S. B. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.20017-x
Additional file 8 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642025
Additional file 5 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642010
Additional file 3 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642004
Additional file 2 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642001
Additional file 4 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642007
Additional file 6 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642019
Additional file 1 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13641998
Additional file 7 of Phylogenetic analysis of the caspase family in bivalves: implications for programmed cell death, immune response and development
Vogeler, S., Carboni, S., Li, X., & Joyce, A. (2021) · Figshare · doi:10.6084/m9.figshare.13642022
Implication de l'inflammasome NLRP3 dans la sécrétion non conventionnelle de la protéine FADD
Mouasni, S. (2018) · theses.fr (ABES) · doi:10.70675/8623f190zbb94z44b7z8b70zd93fa9be484d
Propagation d'un signal pro-apoptotique paracrine via la voie cGAS/STING lors des chimitothérapies antimitotiques
Lohard, S. (2019) · doi:10.70675/10e179e8zfcc6z4481zbb4bzafeef9c41257
Metalloprotease-mediated cleavage of CD95 ligand
Risso, V. (2022) · theses.fr (ABES) · doi:10.70675/36a21870z79bbz4fa6z89edzc2eb46de8295
Caspase-8 homo-oligomerization induces apoptosis and suppresses necroptosis to regulate tissue homeostasisPreprint
Pasparakis, M., Stair, N., Seiler, J., Mannion, J., de Vasconcelos, N. M., Meier, P., Craxton, A., MacFarlane, M., & Wachsmuth, L. (2026) · Research Square · doi:10.21203/rs.3.rs-8701971/v1
Caspase-14 recognizes and processes IL-1β in epithelial cells to drive anti-bacterial IgG productionPreprint
Ma, M., Wang, L., & Ge, B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.14.717951
The regulated cell death nexus: From molecular mechanisms to NINJ1-mediated membrane rupture
Tao, Y., Qiu, T., Zhang, J., Wang, N., & Sun, X. (2026) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2026.05.002
A Noncanonical Model of DED1 Interaction Betweenc-FLIPS and Procaspase-8
Zhu, Z., & Bai, Z.-Q. (2026) · The Protein Journal · doi:10.1007/s10930-026-10335-7
TNF receptor activation through pre-assembly and tonic signaling
Kotaich, F., Jean, M., Tremblais, J., Rucci, P., Logüercho, M., Sica, M., & Legembre, P. (2026) · Trends Open · doi:10.1016/j.treopn.2026.05.006
Pyroptosis across species and its potential impact on host defense against zoonotic pathogens
Ho, S., & Bryant, C. E. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.05.008
Time-Course Transcriptomic Analysis Reveals PANoptosis–CCL2 Axis in Herpes Simplex Keratitis
Wu, C., Ouyang, J., Liu, Y., Zhao, B., Wang, Q. H., Liu, J., Jiang, J., & Hu, K. (2026) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.67.6.38
Epstein–Barr Virus-Mediated Apoptosis Evasion in Epithelial Malignancies: Molecular Mechanisms and Therapeutic Implications
Blanco, R., Soto, C., & Muñoz, J. P. (2026) · Biology · doi:10.3390/biology15141121
Targeting Protein-Protein Interactions in the Extrinsic Apoptotic Pathway and Their Implications in Cancer
Sharma, A., Bhattacharya, N., Srivastava, A., Dutta, S., & Bose, K. (2026) · Microscopy and Microanalysis · doi:10.1093/mam/ozag053.372
Death domain-mediated higher-order oligomerization of RIPK1 drives TNF-induced signaling
Chen, Y., Jianwei, L., Tan, Y. B., Lai, L., Liu, P., Sari, I. N., Raju, A., Huynh, V. T., Velazquez, A. M. V., Yeo, S. J., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01889-1
Stacking Up: The Expanding Catalog of Filament-Forming Enzymes
Horton, N. C. (2026) · Biochemistry · doi:10.1021/acs.biochem.6c00586
SIR2-mediated filament assembly activates the NLR-like protein Avs5 for bacterial antiviral defense
Wang, C., Xie, J., Shen, Z., Ehrmann, J. F., Yu, C., Fang, M., Wu, H., & Fu, T.-M. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118223
Self-citation

Authors: Fu, T.-M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., & Wu, H.
Affiliations: Boston Children's Hospital (US)
Howard Hughes Medical Institute (US)
The University of Queensland (AU)
National Institutes of Health (US)
University of Washington (US)
Texas Medical Center (US)
University of Virginia (US)
Corresponding author: Wu, Hao
ORCID: Fu, Tian-Min
Li, Yang
Lu, Alvin
Li, Zongli
Vajjhala, Parimala R.
Cruz, Anthony C.
DiMaio, Frank
Penczek, Pawel A.
Siegel, Richard M.
Stacey, Katryn J.
Egelman, Edward H.
Wu, Hao
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2016-10
Volume: 64
Issue: 2
Pages: 236-250
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2016.09.009
PMC: PMC5089849
OpenAlex: W2531084658
Cited by: 196
References: 48
Citations by year: 2026: 16 · 2025: 22 · 2024: 24 · 2023: 9 · 2022: 16 · 2021: 35 · 2020: 25 · 2019: 24 · 2018: 13 · 2017: 10 · 2016: 1
FWCI: 8.49
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 384 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Health and Medical Research Council
National Medical Research Council
National Institute of General Medical Sciences (R01GM060635)
National Institute of Allergy and Infectious Diseases (R37AI050872, R01AI045937, R01AI124491)
National Institute of Biomedical Imaging and Bioengineering (R01EB001567)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (DP1HD087988)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: caspase-8, death-inducing signaling complex, FADD, c-FLIP, ASC, inflammasome, death receptor signaling, caspase activation, protein filament assembly, protein-protein interfaces, Fas-mediated apoptosis, caspase inhibition
MeSH terms: Death Effector Domain, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Amino Acid Sequence, Binding Sites, Cytoskeletal Proteins, Humans, Plasmids, Protein Binding, Recombinant Fusion Proteins, Transfection, Viral Proteins, Gene Expression, Sequence Alignment, Apoptosis, Sequence Homology, Amino Acid, fas Receptor, Jurkat Cells, Cryoelectron Microscopy, Caspase 8, Fas-Associated Death Domain Protein, Death Domain Receptor Signaling Adaptor Proteins, CASP8 and FADD-Like Apoptosis Regulating Protein, CARD Signaling Adaptor Proteins, Protein Interaction Domains and Motifs

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Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex

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